A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1.

Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J
J Mol Biol :167174 (2021 Jul 21)
PMID: 34302818
doi: 10.1016/j.jmb.2021.167174
Submitted to SASBDB: 2021 Jun 3
Published in SASBDB:

SASDL56 – 14-3-3 zeta truncated at C-terminus

14-3-3 protein zeta/delta experimental SAS data
14-3-3 protein zeta/delta Kratky plot
Sample: 14-3-3 protein zeta/delta dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
RgGuinier 2.8 nm
Dmax 7.9 nm

SASDLT3 – Ataxin-1 AXH-C

Ataxin-1 experimental SAS data
Ataxin-1 AXH-C Rg histogram
Sample: Ataxin-1 dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
RgGuinier 4.3 nm
Dmax 14.6 nm
VolumePorod 90 nm3

SASDL46 – 14-3-3zeta AXH-C complex

14-3-3 protein zeta/deltaAtaxin-1 AXH-C experimental SAS data
MULTIFOXS model
Sample: 14-3-3 protein zeta/delta dimer, 53 kDa Homo sapiens protein
Ataxin-1 AXH-C dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
RgGuinier 4.8 nm
Dmax 19.8 nm